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| | <StructureSection load='4db6' size='340' side='right'caption='[[4db6]], [[Resolution|resolution]] 1.80Å' scene=''> | | <StructureSection load='4db6' size='340' side='right'caption='[[4db6]], [[Resolution|resolution]] 1.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4db6]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Synthetic_construct_sequences Synthetic construct sequences]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DB6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4DB6 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4db6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DB6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4DB6 FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4db8|4db8]], [[4db9|4db9]], [[4dba|4dba]]</td></tr> | + | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4db6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4db6 OCA], [https://pdbe.org/4db6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4db6 RCSB], [https://www.ebi.ac.uk/pdbsum/4db6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4db6 ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4db6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4db6 OCA], [http://pdbe.org/4db6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4db6 RCSB], [http://www.ebi.ac.uk/pdbsum/4db6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4db6 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Synthetic construct sequences]] | + | [[Category: Synthetic construct]] |
| - | [[Category: Grutter, M G]] | + | [[Category: Grutter MG]] |
| - | [[Category: Madhurantakam, C]] | + | [[Category: Madhurantakam C]] |
| - | [[Category: Mittl, P R.E]] | + | [[Category: Mittl PRE]] |
| - | [[Category: Pluckthun, A]] | + | [[Category: Pluckthun A]] |
| - | [[Category: Varadamsetty, G]] | + | [[Category: Varadamsetty G]] |
| - | [[Category: Armadillo repeat motif]]
| + | |
| - | [[Category: De novo protein]]
| + | |
| - | [[Category: Solenoid repeat]]
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| Structural highlights
Publication Abstract from PubMed
The armadillo domain is a right-handed super-helix of repeating units composed of three alpha-helices each. Armadillo repeat proteins (ArmRPs) are frequently involved in protein-protein interactions, and because of their modular recognition of extended peptide regions they can serve as templates for the design of artificial peptide binding scaffolds. On the basis of sequential and structural analyses, different consensus-designed ArmRPs were synthesized and show high thermodynamic stabilities, compared to naturally occurring ArmRPs. We determined the crystal structures of four full-consensus ArmRPs with three or four identical internal repeats and two different designs for the N- and C-caps. The crystal structures were refined at resolutions ranging from 1.80 to 2.50 A for the above mentioned designs. A redesign of our initial caps was required to obtain well diffracting crystals. However, the structures with the redesigned caps caused domain swapping events between the N-caps. To prevent this domain swap, 9 and 6 point mutations were introduced in the N- and C-caps, respectively. Structural and biophysical analysis showed that this subsequent redesign of the N-cap prevented domain swapping and improved the thermodynamic stability of the proteins. We systematically investigated the best cap combinations. We conclude that designed ArmRPs with optimized caps are intrinsically stable and well-expressed monomeric proteins and that the high-resolution structures provide excellent structural templates for the continuation of the design of sequence-specific modular peptide recognition units based on armadillo repeats.
Structure-based optimization of designed Armadillo-repeat proteins.,Madhurantakam C, Varadamsetty G, Grutter MG, Pluckthun A, Mittl PR Protein Sci. 2012 Jul;21(7):1015-28. doi: 10.1002/pro.2085. Epub 2012 May 24. PMID:22544642[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Madhurantakam C, Varadamsetty G, Grutter MG, Pluckthun A, Mittl PR. Structure-based optimization of designed Armadillo-repeat proteins. Protein Sci. 2012 Jul;21(7):1015-28. doi: 10.1002/pro.2085. Epub 2012 May 24. PMID:22544642 doi:10.1002/pro.2085
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